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Volumn 43, Issue 10, 2008, Pages 1019-1032

Enzyme stability and stabilization-Aqueous and non-aqueous environment

Author keywords

Chemical modification; CLEAs; Enzyme; Immobilization; Reverse micelle; Stability; Surfactant coating

Indexed keywords

BIOCHEMICAL ENGINEERING; CATALYSIS; CATALYSTS; CHEMICAL MODIFICATION; ENZYME IMMOBILIZATION; ENZYMES; FOOD ADDITIVES; GENETIC ENGINEERING; PROTEINS; TECHNOLOGY;

EID: 50849139867     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2008.06.004     Document Type: Review
Times cited : (986)

References (130)
  • 1
    • 34848845831 scopus 로고    scopus 로고
    • Industrial enzymes in bioindustrial sector development: An Indian perspective
    • Chandel A.K., Rudravaram R., Rao L.V., Pogaku R., and Narasu M.L. Industrial enzymes in bioindustrial sector development: An Indian perspective. J Comm Biotechnol 13 (2007) 283-291
    • (2007) J Comm Biotechnol , vol.13 , pp. 283-291
    • Chandel, A.K.1    Rudravaram, R.2    Rao, L.V.3    Pogaku, R.4    Narasu, M.L.5
  • 2
    • 0029162070 scopus 로고
    • Understanding and increasing protein stability
    • Fagain O. Understanding and increasing protein stability. Biochem Biophys Acta 1252 (1995) 1-14
    • (1995) Biochem Biophys Acta , vol.1252 , pp. 1-14
    • Fagain, O.1
  • 3
    • 77957023432 scopus 로고    scopus 로고
    • Diagnosing the inactivating process of enzymes
    • Ballesteros A., Plou F.J., Iborra J.L., and Halling P.J. (Eds), Elsevier Science B.V, Amsterdam, The Netherlands
    • Misset O., and van Dijk A. Diagnosing the inactivating process of enzymes. In: Ballesteros A., Plou F.J., Iborra J.L., and Halling P.J. (Eds). Stability and stabilization of biocatalysts. Progress in biotechnology vol. 15 (1998), Elsevier Science B.V, Amsterdam, The Netherlands 3-18
    • (1998) Stability and stabilization of biocatalysts. Progress in biotechnology , vol.15 , pp. 3-18
    • Misset, O.1    van Dijk, A.2
  • 4
    • 0002883588 scopus 로고
    • Stabilized soluble enzymes
    • Schmid R. Stabilized soluble enzymes. Adv Biochem Eng 12 (1979) 41-118
    • (1979) Adv Biochem Eng , vol.12 , pp. 41-118
    • Schmid, R.1
  • 5
    • 33747120183 scopus 로고    scopus 로고
    • Thermal and pH inactivation of an immobilized thermostable β-galactosidase from Thermus sp. strain T2: comparison to the free enzyme
    • Ladero M., Ruiz G., Pessela B.C., Viand A., Santos A., and Garcia-Ochoa F. Thermal and pH inactivation of an immobilized thermostable β-galactosidase from Thermus sp. strain T2: comparison to the free enzyme. Biochem Eng J 31 (2006) 14-24
    • (2006) Biochem Eng J , vol.31 , pp. 14-24
    • Ladero, M.1    Ruiz, G.2    Pessela, B.C.3    Viand, A.4    Santos, A.5    Garcia-Ochoa, F.6
  • 6
    • 0027006791 scopus 로고
    • Effect of subunit dissociation, denaturation, aggregation, coagulation and decomposition on enzyme inactivation kinetics: I. First order behavior
    • Lencki R.W., Arul J., and Neufeld R.J. Effect of subunit dissociation, denaturation, aggregation, coagulation and decomposition on enzyme inactivation kinetics: I. First order behavior. Biotechnol Bioeng 40 (1992) 1421-1426
    • (1992) Biotechnol Bioeng , vol.40 , pp. 1421-1426
    • Lencki, R.W.1    Arul, J.2    Neufeld, R.J.3
  • 7
    • 0026970477 scopus 로고
    • Effect of subunit dissociation, denaturation, aggregation, coagulation and decomposition on enzyme inactivation kinetics: II. Biphasic and grace period behavior
    • Lencki R.W., Arul J., and Neufeld R.J. Effect of subunit dissociation, denaturation, aggregation, coagulation and decomposition on enzyme inactivation kinetics: II. Biphasic and grace period behavior. Biotechnol Bioeng 40 (1992) 1427-1434
    • (1992) Biotechnol Bioeng , vol.40 , pp. 1427-1434
    • Lencki, R.W.1    Arul, J.2    Neufeld, R.J.3
  • 8
    • 0023435073 scopus 로고
    • Single-step unimolecular non-first order enzyme inactivation kinetics
    • Sadana A., and Henley J.P. Single-step unimolecular non-first order enzyme inactivation kinetics. Biotechnol Bioeng 30 (1987) 717-723
    • (1987) Biotechnol Bioeng , vol.30 , pp. 717-723
    • Sadana, A.1    Henley, J.P.2
  • 9
    • 27844446141 scopus 로고    scopus 로고
    • Kinetic modelling of the thermal inactivation of an industrial β-galactosidase from Kluyveromyces fragilis
    • Ladero M., Santos A., and Garci{dotless}a-Ochoa F. Kinetic modelling of the thermal inactivation of an industrial β-galactosidase from Kluyveromyces fragilis. Enzyme Microb Technol 38 (2006) 1-9
    • (2006) Enzyme Microb Technol , vol.38 , pp. 1-9
    • Ladero, M.1    Santos, A.2    Garcia-Ochoa, F.3
  • 10
    • 0020999167 scopus 로고
    • Stabilization of enzymes against thermal inactivation
    • Klibanov A.M. Stabilization of enzymes against thermal inactivation. Adv Appl Microbiol 29 (1983) 1-28
    • (1983) Adv Appl Microbiol , vol.29 , pp. 1-28
    • Klibanov, A.M.1
  • 11
    • 3242787913 scopus 로고    scopus 로고
    • Illanes A. "Stability of Biocatalyst", Electr J Biotech (online) ISSN:0717-3458, doi:10.2225/vol2-issue1-fulltext-2.
    • Illanes A. "Stability of Biocatalyst", Electr J Biotech (online) ISSN:0717-3458, doi:10.2225/vol2-issue1-fulltext-2.
  • 12
    • 50849138872 scopus 로고    scopus 로고
    • The effect of crosslinking in thermal inactivation of cellulases
    • Ballesteros A., Plou F.J., Iborra J.L., and Halling P.J. (Eds), Elsevier Science B.V., Amsterdam, The Netherlands
    • Bilen J., and Bakir U. The effect of crosslinking in thermal inactivation of cellulases. In: Ballesteros A., Plou F.J., Iborra J.L., and Halling P.J. (Eds). Stability and stabilization of biocatalysts. Progress in biotechnology vol. 15 (1998), Elsevier Science B.V., Amsterdam, The Netherlands 151-156
    • (1998) Stability and stabilization of biocatalysts. Progress in biotechnology , vol.15 , pp. 151-156
    • Bilen, J.1    Bakir, U.2
  • 14
    • 0034734270 scopus 로고    scopus 로고
    • Halophilic enzymes: proteins with a grain of salt
    • Mevarech M., Frolow F., and Gloss L.M. Halophilic enzymes: proteins with a grain of salt. Biophys Chem 86 (2000) 155-164
    • (2000) Biophys Chem , vol.86 , pp. 155-164
    • Mevarech, M.1    Frolow, F.2    Gloss, L.M.3
  • 15
    • 0035108407 scopus 로고    scopus 로고
    • Enzymes which are stable in the presence of organic solvents
    • Ogino H., and Ishikawa H. Enzymes which are stable in the presence of organic solvents. J Biosci Bioeng 91 (2001) 109-116
    • (2001) J Biosci Bioeng , vol.91 , pp. 109-116
    • Ogino, H.1    Ishikawa, H.2
  • 16
    • 0024278258 scopus 로고
    • Enzymatic catalysis in nonaqueous solvents
    • Zaks A., and Klibanov A.M. Enzymatic catalysis in nonaqueous solvents. J Biol Chem 263 (1988) 3194-3201
    • (1988) J Biol Chem , vol.263 , pp. 3194-3201
    • Zaks, A.1    Klibanov, A.M.2
  • 17
    • 0006645334 scopus 로고    scopus 로고
    • Engineering stability of enzymes in systems with organic solvents
    • Ballesteros A., Plou F.J., Iborra J.L., and Halling P.J. (Eds), Elsevier Science B.V., Amsterdam, The Netherlands
    • Mozhaev V.V. Engineering stability of enzymes in systems with organic solvents. In: Ballesteros A., Plou F.J., Iborra J.L., and Halling P.J. (Eds). Stability and stabilization of biocatalysts. Progress in biotechnology vol. 15 (1998), Elsevier Science B.V., Amsterdam, The Netherlands 355-363
    • (1998) Stability and stabilization of biocatalysts. Progress in biotechnology , vol.15 , pp. 355-363
    • Mozhaev, V.V.1
  • 18
    • 0002284639 scopus 로고    scopus 로고
    • Specialty enzymes from marine microorganisms
    • Haard N. Specialty enzymes from marine microorganisms. Food Technol 52 (1998) 64-67
    • (1998) Food Technol , vol.52 , pp. 64-67
    • Haard, N.1
  • 19
    • 0034913744 scopus 로고    scopus 로고
    • Biotechnological uses of archaeal extremozymes
    • Eichler J. Biotechnological uses of archaeal extremozymes. Biotechnol Adv 19 (2001) 261-278
    • (2001) Biotechnol Adv , vol.19 , pp. 261-278
    • Eichler, J.1
  • 20
    • 0021371442 scopus 로고
    • Structure-stability relationships in proteins: new approaches to stabilizing enzymes
    • Mozhaev V.V., and Martinek K. Structure-stability relationships in proteins: new approaches to stabilizing enzymes. Enzyme Microb Technol 6 (1984) 50-59
    • (1984) Enzyme Microb Technol , vol.6 , pp. 50-59
    • Mozhaev, V.V.1    Martinek, K.2
  • 21
    • 17644365489 scopus 로고    scopus 로고
    • Structural features of thermozymes
    • Li W.F., Zhou X.X., and Lu P. Structural features of thermozymes. Biotechnol Adv 23 (2005) 271-281
    • (2005) Biotechnol Adv , vol.23 , pp. 271-281
    • Li, W.F.1    Zhou, X.X.2    Lu, P.3
  • 22
    • 0037070488 scopus 로고    scopus 로고
    • Studies on the activity and the stability of β-galactosidases from Thermus sp strain T2 and from Kluyveromyces fragilis
    • Ladero M., Santos A., Garci{dotless}a J.L., Carrascosa A.V., Pessela B.C., and Garci{dotless}a-Ochoa F. Studies on the activity and the stability of β-galactosidases from Thermus sp strain T2 and from Kluyveromyces fragilis. Enzyme Microb Technol 30 (2002) 392-405
    • (2002) Enzyme Microb Technol , vol.30 , pp. 392-405
    • Ladero, M.1    Santos, A.2    Garcia, J.L.3    Carrascosa, A.V.4    Pessela, B.C.5    Garcia-Ochoa, F.6
  • 23
    • 0642368518 scopus 로고    scopus 로고
    • Production of β-xylanase and β-xylosidase by the extremely halophilic archaeon Halorhabdus utahensis
    • Waino M., and Ingvorsen K. Production of β-xylanase and β-xylosidase by the extremely halophilic archaeon Halorhabdus utahensis. Extremophiles 7 (2003) 87-93
    • (2003) Extremophiles , vol.7 , pp. 87-93
    • Waino, M.1    Ingvorsen, K.2
  • 24
    • 34248190092 scopus 로고    scopus 로고
    • Improving the umami taste of soy sauce by the addition of bacterial γ-glutamyltranspeptidase as a glutaminase to the fermentation mixture
    • Kijima K., and Suzuki H. Improving the umami taste of soy sauce by the addition of bacterial γ-glutamyltranspeptidase as a glutaminase to the fermentation mixture. Enzyme Microb Technol 41 (2007) 80-84
    • (2007) Enzyme Microb Technol , vol.41 , pp. 80-84
    • Kijima, K.1    Suzuki, H.2
  • 25
    • 40749113133 scopus 로고    scopus 로고
    • Production of glutaminase (E.C.3.2.1.5) from Zygosaccharomyces rouxii: statistical optimization using response surface methodology
    • Iyer P., and Singhal R.S. Production of glutaminase (E.C.3.2.1.5) from Zygosaccharomyces rouxii: statistical optimization using response surface methodology. Bioresource Technol 99 (2008) 4300-4307
    • (2008) Bioresource Technol , vol.99 , pp. 4300-4307
    • Iyer, P.1    Singhal, R.S.2
  • 26
    • 28344445175 scopus 로고    scopus 로고
    • Characterization of salt-tolerant glutaminase from Stenotrophomonas maltophilia NYW-81 and its application in Japanese soy sauce fermentation
    • Wakayama M., Yamagata T., Kamemura A., Bootim N., Yano S., Tachiki T., et al. Characterization of salt-tolerant glutaminase from Stenotrophomonas maltophilia NYW-81 and its application in Japanese soy sauce fermentation. J Ind Microbiol Biotechnol 32 (2005) 383-390
    • (2005) J Ind Microbiol Biotechnol , vol.32 , pp. 383-390
    • Wakayama, M.1    Yamagata, T.2    Kamemura, A.3    Bootim, N.4    Yano, S.5    Tachiki, T.6
  • 28
    • 0029893110 scopus 로고    scopus 로고
    • Thermozymes identifying molecular determinants of protein structural and functional stability
    • Vieille C., and Zekus J. Thermozymes identifying molecular determinants of protein structural and functional stability. Trends Biotechnol 14 (1996) 183-190
    • (1996) Trends Biotechnol , vol.14 , pp. 183-190
    • Vieille, C.1    Zekus, J.2
  • 29
    • 0041430569 scopus 로고    scopus 로고
    • Chemical modification of biocatalysts
    • Davis B.G. Chemical modification of biocatalysts. Curr Opinion Biotechnol 14 (2003) 379-386
    • (2003) Curr Opinion Biotechnol , vol.14 , pp. 379-386
    • Davis, B.G.1
  • 30
    • 0029311202 scopus 로고
    • Strategies for enzyme stabilization by intramolecular crosslinking with bifunctional reagents
    • Fernandez-Lafuente R., Rosell C., Rodriguez V., and Guisan J. Strategies for enzyme stabilization by intramolecular crosslinking with bifunctional reagents. Enzyme Microb Technol 17 (1995) 517-523
    • (1995) Enzyme Microb Technol , vol.17 , pp. 517-523
    • Fernandez-Lafuente, R.1    Rosell, C.2    Rodriguez, V.3    Guisan, J.4
  • 31
    • 13844321001 scopus 로고    scopus 로고
    • Stabilization of a-chymotrypsin by chemical modification with monoamine cyclodextrin
    • Fernandez M., Fragoso A., Cao R., and Villalong R. Stabilization of a-chymotrypsin by chemical modification with monoamine cyclodextrin. Process Biochem 40 (2005) 2091-2094
    • (2005) Process Biochem , vol.40 , pp. 2091-2094
    • Fernandez, M.1    Fragoso, A.2    Cao, R.3    Villalong, R.4
  • 33
    • 84948967568 scopus 로고
    • Enzyme stabilization by multipoint covalent attachment to activated pre-existing supports
    • van der Tweel W., Harder A., and Buitelar R. (Eds), Elsevier, Amsterdam
    • Guisan J., Fernandez-Lafuente R., Rodriguez V., Bastida A., and Alvaro G. Enzyme stabilization by multipoint covalent attachment to activated pre-existing supports. In: van der Tweel W., Harder A., and Buitelar R. (Eds). Stability and stabilization of enzymes (1993), Elsevier, Amsterdam 55-62
    • (1993) Stability and stabilization of enzymes , pp. 55-62
    • Guisan, J.1    Fernandez-Lafuente, R.2    Rodriguez, V.3    Bastida, A.4    Alvaro, G.5
  • 34
    • 0022011347 scopus 로고
    • Enzyme stabilization towards chemical, thermal and proteolytic deactivation
    • Gianfreda L., Modafferi M., and Greco Jr. G. Enzyme stabilization towards chemical, thermal and proteolytic deactivation. Enzyme Microb Technol 7 (1985) 78-82
    • (1985) Enzyme Microb Technol , vol.7 , pp. 78-82
    • Gianfreda, L.1    Modafferi, M.2    Greco Jr., G.3
  • 36
    • 0034003045 scopus 로고    scopus 로고
    • Immobilization of functionally unstable catechol-2,3-dioxygenase greatly improves operational stability
    • Fernandez-Lafuente R., Guisan J.M., Alib S., and Cowan D. Immobilization of functionally unstable catechol-2,3-dioxygenase greatly improves operational stability. Enzyme Microb Technol 26 (2000) 568-573
    • (2000) Enzyme Microb Technol , vol.26 , pp. 568-573
    • Fernandez-Lafuente, R.1    Guisan, J.M.2    Alib, S.3    Cowan, D.4
  • 37
    • 0029626674 scopus 로고
    • Hyperstabilization of a thermophilic esterase by multipoint covalent attachment
    • Fernandez-Lafuente R., Cowan D., and Wood A. Hyperstabilization of a thermophilic esterase by multipoint covalent attachment. Enzyme Microb Technol 17 (1995) 366-372
    • (1995) Enzyme Microb Technol , vol.17 , pp. 366-372
    • Fernandez-Lafuente, R.1    Cowan, D.2    Wood, A.3
  • 39
    • 33646500582 scopus 로고    scopus 로고
    • Glyoxyl agarose: a fully inert and hydrophilic support for immobilization and high stabilization of proteins
    • Mateo C., Palomo J.M., Fuentes M., Betancor L., Grazu V., Lopez-Gallego F., et al. Glyoxyl agarose: a fully inert and hydrophilic support for immobilization and high stabilization of proteins. Enzyme Microb Technol 39 (2006) 274-280
    • (2006) Enzyme Microb Technol , vol.39 , pp. 274-280
    • Mateo, C.1    Palomo, J.M.2    Fuentes, M.3    Betancor, L.4    Grazu, V.5    Lopez-Gallego, F.6
  • 41
    • 21644461452 scopus 로고    scopus 로고
    • Immobilization and stabilization of glutaryl acylase on aminated sepabeads supports by the glutaraldehyde crosslinking method
    • Alonso N., Lopez-Gallego F., Betancor L., Hidalgo A., Mateo C., Guisan J.M., et al. Immobilization and stabilization of glutaryl acylase on aminated sepabeads supports by the glutaraldehyde crosslinking method. J Mol Catal B: Enzymatic 35 (2005) 57-61
    • (2005) J Mol Catal B: Enzymatic , vol.35 , pp. 57-61
    • Alonso, N.1    Lopez-Gallego, F.2    Betancor, L.3    Hidalgo, A.4    Mateo, C.5    Guisan, J.M.6
  • 42
    • 15744373608 scopus 로고    scopus 로고
    • Immobilization and stabilization of pullulanase from Klebsiella pneumoniae by a multipoint attachment method using activated agar gel supports
    • Kuroiwa T., Shoda H., Ichikawa S., Sato S., and Mukataka S. Immobilization and stabilization of pullulanase from Klebsiella pneumoniae by a multipoint attachment method using activated agar gel supports. Process Biochem 40 (2005) 2637-2642
    • (2005) Process Biochem , vol.40 , pp. 2637-2642
    • Kuroiwa, T.1    Shoda, H.2    Ichikawa, S.3    Sato, S.4    Mukataka, S.5
  • 43
    • 28844472482 scopus 로고    scopus 로고
    • Direct immobilization of peroxidase on DEAE cellulose from ammonium sulphate fractionated proteins of bitter gourd (Momordica charantia)
    • Kulshrestha Y., and Husain Q. Direct immobilization of peroxidase on DEAE cellulose from ammonium sulphate fractionated proteins of bitter gourd (Momordica charantia). Enzyme Microb Technol 38 (2006) 470-477
    • (2006) Enzyme Microb Technol , vol.38 , pp. 470-477
    • Kulshrestha, Y.1    Husain, Q.2
  • 45
  • 46
    • 43149108336 scopus 로고    scopus 로고
    • Chan L, Cross HF, She JK, Cavalli G, Martins HFP, Neylon C. Covalent attachment of proteins to solid supports and surfaces via Sortase-mediated ligation. PLoS ONE 2007;2(11): e1164. doi:10.1371/journal.pone.0001164.
    • Chan L, Cross HF, She JK, Cavalli G, Martins HFP, Neylon C. Covalent attachment of proteins to solid supports and surfaces via Sortase-mediated ligation. PLoS ONE 2007;2(11): e1164. doi:10.1371/journal.pone.0001164.
  • 47
    • 7544220924 scopus 로고
    • Immobilised enzymes as drugs
    • Torchilin V.P. Immobilised enzymes as drugs. Adv Drug Deliv Rev 1 (1988) 270
    • (1988) Adv Drug Deliv Rev , vol.1 , pp. 270
    • Torchilin, V.P.1
  • 48
    • 38149059723 scopus 로고    scopus 로고
    • Immobilization-stabilization of an α-galactosidase from Thermus sp. strain T2 by covalent immobilization on highly activated supports: selection of the optimal immobilization strategy
    • Filho M., Pessela B.C., Mateo C., Carrascosa A.V., Fernandez-Lafuente R., and Guisan J.M. Immobilization-stabilization of an α-galactosidase from Thermus sp. strain T2 by covalent immobilization on highly activated supports: selection of the optimal immobilization strategy. Enzyme Microb Technol 42 (2008) 265-271
    • (2008) Enzyme Microb Technol , vol.42 , pp. 265-271
    • Filho, M.1    Pessela, B.C.2    Mateo, C.3    Carrascosa, A.V.4    Fernandez-Lafuente, R.5    Guisan, J.M.6
  • 49
    • 34548392243 scopus 로고    scopus 로고
    • Improvement of the stability of glucose oxidase via encapsulation in sodium alginate-cellulose sulfate-poly(methylene-co-guanidine) capsules
    • Vikartovska A., Bucko M., Mislovicova D., Patoprsty V., Laci{dotless}k I., and Gemeiner P. Improvement of the stability of glucose oxidase via encapsulation in sodium alginate-cellulose sulfate-poly(methylene-co-guanidine) capsules. Enzyme Microb Technol 41 (2007) 748-755
    • (2007) Enzyme Microb Technol , vol.41 , pp. 748-755
    • Vikartovska, A.1    Bucko, M.2    Mislovicova, D.3    Patoprsty, V.4    Lacik, I.5    Gemeiner, P.6
  • 50
    • 33947594941 scopus 로고    scopus 로고
    • Immobilization of enzymes into nanocavities for the improvement of biosensor stability
    • Vamvakaki V., and Chaniotakis N.A. Immobilization of enzymes into nanocavities for the improvement of biosensor stability. Biosens Bioelectronics 22 (2007) 2650-2655
    • (2007) Biosens Bioelectronics , vol.22 , pp. 2650-2655
    • Vamvakaki, V.1    Chaniotakis, N.A.2
  • 51
    • 27844518415 scopus 로고    scopus 로고
    • Nanostructures for enzyme stabilization
    • Kim J., Grate J.W., and Wang P. Nanostructures for enzyme stabilization. Chem Eng Sci 61 (2006) 1017-1026
    • (2006) Chem Eng Sci , vol.61 , pp. 1017-1026
    • Kim, J.1    Grate, J.W.2    Wang, P.3
  • 52
    • 33748782565 scopus 로고    scopus 로고
    • Stabilization of glucoso-6-phosphate dehydrogenase by its substrate and cofactor in an ultrasonic field
    • Karaseva E., and Metelitza D. Stabilization of glucoso-6-phosphate dehydrogenase by its substrate and cofactor in an ultrasonic field. Russ J Bioorg Chem 32 (2006) 436-443
    • (2006) Russ J Bioorg Chem , vol.32 , pp. 436-443
    • Karaseva, E.1    Metelitza, D.2
  • 53
    • 21844431597 scopus 로고    scopus 로고
    • Testing polyols' compatibility with Gibbs energy of stabilization of proteins under conditions in which they behave as compatible osmolytes
    • Haque I., Singh R., Ahmad F., and Moosavi-Movahedi A. Testing polyols' compatibility with Gibbs energy of stabilization of proteins under conditions in which they behave as compatible osmolytes. FEBS Lett 579 (2005) 3891-3898
    • (2005) FEBS Lett , vol.579 , pp. 3891-3898
    • Haque, I.1    Singh, R.2    Ahmad, F.3    Moosavi-Movahedi, A.4
  • 54
    • 28844470977 scopus 로고    scopus 로고
    • Acidic and proteolytic digestion of α-amylases from Bacillus licheniformis and Bacillus amyloliquefaciens: stability and flexibility analysis
    • Khajeh K., Shokri M.M., Asghari S.M., Moradian F., Ghasemi A., Sadeghi M., et al. Acidic and proteolytic digestion of α-amylases from Bacillus licheniformis and Bacillus amyloliquefaciens: stability and flexibility analysis. Enzyme Microb Technol 38 (2006) 422-428
    • (2006) Enzyme Microb Technol , vol.38 , pp. 422-428
    • Khajeh, K.1    Shokri, M.M.2    Asghari, S.M.3    Moradian, F.4    Ghasemi, A.5    Sadeghi, M.6
  • 55
    • 0030271204 scopus 로고    scopus 로고
    • Comparative thermostability of glucose dehydrogenase from Haloferax mediterranei. Effects of salts and polyols
    • Obon J.M., Manjon A., and Iborra J.L. Comparative thermostability of glucose dehydrogenase from Haloferax mediterranei. Effects of salts and polyols. Enzyme Microb Technol 19 (1996) 352-360
    • (1996) Enzyme Microb Technol , vol.19 , pp. 352-360
    • Obon, J.M.1    Manjon, A.2    Iborra, J.L.3
  • 56
    • 0035071613 scopus 로고    scopus 로고
    • A novel thermostable xylanase from Thermosmonospora sp.: influence of additives on thermostability
    • George S.P., Ahmad A., and Rao M.L. A novel thermostable xylanase from Thermosmonospora sp.: influence of additives on thermostability. Bioresour Technol 78 (2001) 221-224
    • (2001) Bioresour Technol , vol.78 , pp. 221-224
    • George, S.P.1    Ahmad, A.2    Rao, M.L.3
  • 57
    • 0023905575 scopus 로고
    • The mechanism of cryoprotection of proteins by solutes
    • Carpenter J.F., and Crowe J.H. The mechanism of cryoprotection of proteins by solutes. Cryobiology 25 (1988) 244-255
    • (1988) Cryobiology , vol.25 , pp. 244-255
    • Carpenter, J.F.1    Crowe, J.H.2
  • 58
    • 0021675149 scopus 로고
    • Effect of polyhydric alcohol on invertase stabilization
    • Monsan D., and Coombes P. Effect of polyhydric alcohol on invertase stabilization. Ann N Y Acad Sci 434 (1984) 61-64
    • (1984) Ann N Y Acad Sci , vol.434 , pp. 61-64
    • Monsan, D.1    Coombes, P.2
  • 59
    • 23744434321 scopus 로고    scopus 로고
    • Activation and stabilization of 10 starch-degrading enzymes by Triton X-100, polyethylene glycols, and polyvinyl alcohols
    • Yoon S., and Robyt J.F. Activation and stabilization of 10 starch-degrading enzymes by Triton X-100, polyethylene glycols, and polyvinyl alcohols. Enzyme Microb Technol 37 (2005) 556-562
    • (2005) Enzyme Microb Technol , vol.37 , pp. 556-562
    • Yoon, S.1    Robyt, J.F.2
  • 61
    • 14544267631 scopus 로고    scopus 로고
    • Stabilization method of an alkaline protease from inactivation by heat SDS and hydrogen peroxide
    • Joo H., Koo Y., Choi J., and Changa C. Stabilization method of an alkaline protease from inactivation by heat SDS and hydrogen peroxide. Enzyme Microb Technol 36 (2005) 766-772
    • (2005) Enzyme Microb Technol , vol.36 , pp. 766-772
    • Joo, H.1    Koo, Y.2    Choi, J.3    Changa, C.4
  • 62
    • 0345528075 scopus 로고    scopus 로고
    • Effect of β-cyclodextrin-polysucrose polymer on the stability properties of soluble trypsin
    • Fernandez M., Villalonga M.L., Fragoso A., Cao R., and Villalonga R. Effect of β-cyclodextrin-polysucrose polymer on the stability properties of soluble trypsin. Enzyme Microb Technol 34 (2004) 78-82
    • (2004) Enzyme Microb Technol , vol.34 , pp. 78-82
    • Fernandez, M.1    Villalonga, M.L.2    Fragoso, A.3    Cao, R.4    Villalonga, R.5
  • 63
    • 0032669215 scopus 로고    scopus 로고
    • Protein stabilising effect of polyethyleneimine
    • Andersson M.M., and Hatti-Kaul R. Protein stabilising effect of polyethyleneimine. J Biotechnol 72 (1999) 21-31
    • (1999) J Biotechnol , vol.72 , pp. 21-31
    • Andersson, M.M.1    Hatti-Kaul, R.2
  • 65
    • 0037473475 scopus 로고    scopus 로고
    • Stabilisation and determination of the biological activity of l-asparaginase in poly(d,l-lactide-co-glycolide) nanospheres
    • Wolf M., Wirth M., Pittner F., and Gabor F. Stabilisation and determination of the biological activity of l-asparaginase in poly(d,l-lactide-co-glycolide) nanospheres. Int J Pharm 256 (2003) 141-152
    • (2003) Int J Pharm , vol.256 , pp. 141-152
    • Wolf, M.1    Wirth, M.2    Pittner, F.3    Gabor, F.4
  • 66
    • 0037413454 scopus 로고    scopus 로고
    • Stabilisation of enzymes with polyvinylsaccharides I: physical stabilisation of horseradish peroxidase
    • Kuhlmeyer C., and Klein J. Stabilisation of enzymes with polyvinylsaccharides I: physical stabilisation of horseradish peroxidase. Enzyme Microb Technol 32 (2003) 99-106
    • (2003) Enzyme Microb Technol , vol.32 , pp. 99-106
    • Kuhlmeyer, C.1    Klein, J.2
  • 67
    • 22544487194 scopus 로고    scopus 로고
    • Stabilization of α-amylase by using anionic surfactant during the immobilization process
    • El-Batal A.I., Atia K.S., and Eid M. Stabilization of α-amylase by using anionic surfactant during the immobilization process. Radiat Phy Chem 74 (2005) 96-101
    • (2005) Radiat Phy Chem , vol.74 , pp. 96-101
    • El-Batal, A.I.1    Atia, K.S.2    Eid, M.3
  • 69
    • 0035725911 scopus 로고    scopus 로고
    • Production, purification, characterization and application of lipases
    • Sharma R., Chisti Y., and Banerjee U.C. Production, purification, characterization and application of lipases. Biotechnol Adv 19 (2001) 627-662
    • (2001) Biotechnol Adv , vol.19 , pp. 627-662
    • Sharma, R.1    Chisti, Y.2    Banerjee, U.C.3
  • 70
    • 0028808177 scopus 로고
    • Organic solvent tolerant bacterium which secretes an organic solvent-stable proteolytic enzyme
    • Ogino H., Yusui K., Shiotani T., Ishihara T., and Ishikawa H. Organic solvent tolerant bacterium which secretes an organic solvent-stable proteolytic enzyme. Appl Environ Microbiol 61 (1995) 4258-4262
    • (1995) Appl Environ Microbiol , vol.61 , pp. 4258-4262
    • Ogino, H.1    Yusui, K.2    Shiotani, T.3    Ishihara, T.4    Ishikawa, H.5
  • 71
    • 0033199021 scopus 로고    scopus 로고
    • Biocatalysis in organic media using enzymes from extremophiles
    • Sellek A.G., and Chaudhuri J.B. Biocatalysis in organic media using enzymes from extremophiles. Enzyme Microb Technol 25 (1999) 471-482
    • (1999) Enzyme Microb Technol , vol.25 , pp. 471-482
    • Sellek, A.G.1    Chaudhuri, J.B.2
  • 72
    • 50849098852 scopus 로고    scopus 로고
    • Stabilization of hydrolases by chemical modification with fatty acids or polyethylene glycol
    • Ballesteros A., Plou F.J., Iborra J.L., and Halling P.J. (Eds), Elsevier Science B.V., Amsterdam, The Netherlands
    • Plou F.J., Calvo M.V., Ferrer M., and Ballesteros A. Stabilization of hydrolases by chemical modification with fatty acids or polyethylene glycol. In: Ballesteros A., Plou F.J., Iborra J.L., and Halling P.J. (Eds). Stability and stabilization of biocatalysts. Progress in biotechnology vol. 15 (1998), Elsevier Science B.V., Amsterdam, The Netherlands 115-120
    • (1998) Stability and stabilization of biocatalysts. Progress in biotechnology , vol.15 , pp. 115-120
    • Plou, F.J.1    Calvo, M.V.2    Ferrer, M.3    Ballesteros, A.4
  • 73
    • 0029256724 scopus 로고
    • Biomedical and Biotechnological applications of PEG and PM modified proteins
    • Inada Y., Furukawa M., Sasaki H., Kodera Y., Hiroto M., Nishimura H., et al. Biomedical and Biotechnological applications of PEG and PM modified proteins. TIBTECH 13 (1995) 86-91
    • (1995) TIBTECH , vol.13 , pp. 86-91
    • Inada, Y.1    Furukawa, M.2    Sasaki, H.3    Kodera, Y.4    Hiroto, M.5    Nishimura, H.6
  • 74
    • 24944436422 scopus 로고    scopus 로고
    • Activity and stability of Caldariomyces fumago chloroperoxidase modified by reductive alkylation, amidation and cross-linking
    • La Rotta Hernandez C.E., Lutz S., Liese A., and Bon E.P.S. Activity and stability of Caldariomyces fumago chloroperoxidase modified by reductive alkylation, amidation and cross-linking. Enzyme Microb Technol 37 (2005) 582-588
    • (2005) Enzyme Microb Technol , vol.37 , pp. 582-588
    • La Rotta Hernandez, C.E.1    Lutz, S.2    Liese, A.3    Bon, E.P.S.4
  • 75
    • 0025405523 scopus 로고
    • Multipoint attachment to a support protects enzyme from inactivation by organic solvents: (-chymotrypsin in aqueous solutions of alcohols and diols
    • Mozhaev V.V., Sergeeva M.V., Belova A.B., and Khmelnitsky Y.L. Multipoint attachment to a support protects enzyme from inactivation by organic solvents: (-chymotrypsin in aqueous solutions of alcohols and diols. Biotechnol Bioeng 35 (1989) 653-659
    • (1989) Biotechnol Bioeng , vol.35 , pp. 653-659
    • Mozhaev, V.V.1    Sergeeva, M.V.2    Belova, A.B.3    Khmelnitsky, Y.L.4
  • 76
    • 18644365066 scopus 로고    scopus 로고
    • Preparation of artificial hyper-hydrophilic micro-environments (polymeric salts) surrounding enzyme molecules: new enzyme derivatives to be used in any reaction medium
    • Abian O., Wilson L., Mateo C., Fernandez-Lorente G., Palomo J.M., Fernandez-Lafuente R., et al. Preparation of artificial hyper-hydrophilic micro-environments (polymeric salts) surrounding enzyme molecules: new enzyme derivatives to be used in any reaction medium. J Mol Catal B: Enzymatic 19-20 (2002) 295-303
    • (2002) J Mol Catal B: Enzymatic , vol.19-20 , pp. 295-303
    • Abian, O.1    Wilson, L.2    Mateo, C.3    Fernandez-Lorente, G.4    Palomo, J.M.5    Fernandez-Lafuente, R.6
  • 77
    • 23244433762 scopus 로고    scopus 로고
    • The use of poly (ethylene oxide) for the efficient stabilization of entrapped a-chymotrypsin in silicone elastomers: a chemometric study
    • Ragheb A.M., Hileman O.E., and Brook M. The use of poly (ethylene oxide) for the efficient stabilization of entrapped a-chymotrypsin in silicone elastomers: a chemometric study. Biomaterials 26 (2005) 6973-6983
    • (2005) Biomaterials , vol.26 , pp. 6973-6983
    • Ragheb, A.M.1    Hileman, O.E.2    Brook, M.3
  • 78
    • 0032890111 scopus 로고    scopus 로고
    • Facile synthesis of artificial enzyme nano-environments via solid-phase chemistry of immobilized derivatives: dramatic stabilization of penicillin acylase versus organic solvents
    • Fernandez-Lafuente R., Rosell C.M., Caanan-Haden L., Rodes L., and Guisan J.M. Facile synthesis of artificial enzyme nano-environments via solid-phase chemistry of immobilized derivatives: dramatic stabilization of penicillin acylase versus organic solvents. Enzyme Microb Technol 24 (1999) 96-103
    • (1999) Enzyme Microb Technol , vol.24 , pp. 96-103
    • Fernandez-Lafuente, R.1    Rosell, C.M.2    Caanan-Haden, L.3    Rodes, L.4    Guisan, J.M.5
  • 79
    • 0035210770 scopus 로고    scopus 로고
    • Stabilization of immobilized enzymes against water-soluble organic cosolvents and generation of hyperhydrophilic micro-environments surrounding enzyme molecules
    • Abian O., Mateo C., Fernandez-Lorente G., Palomo J.M., Fernandez-Lafuente R., and Guisan J.M. Stabilization of immobilized enzymes against water-soluble organic cosolvents and generation of hyperhydrophilic micro-environments surrounding enzyme molecules. Biocatal Biotrans 19 (2001) 489-503
    • (2001) Biocatal Biotrans , vol.19 , pp. 489-503
    • Abian, O.1    Mateo, C.2    Fernandez-Lorente, G.3    Palomo, J.M.4    Fernandez-Lafuente, R.5    Guisan, J.M.6
  • 80
    • 0037072993 scopus 로고    scopus 로고
    • Stabilization of horseradish peroxidase in aqueous-organic media by immobilization onto cellulose using a cellulose-binding-domain
    • Fishman A., Levy I., Cogan U., and Shoseyov O. Stabilization of horseradish peroxidase in aqueous-organic media by immobilization onto cellulose using a cellulose-binding-domain. J Mol Catal B: Enzymatic 18 (2002) 121-131
    • (2002) J Mol Catal B: Enzymatic , vol.18 , pp. 121-131
    • Fishman, A.1    Levy, I.2    Cogan, U.3    Shoseyov, O.4
  • 82
    • 33846143530 scopus 로고    scopus 로고
    • Genetic modification of the Penicillin G Acylase surface to improve its reversible immobilization on ionic exchangers
    • Montes T., Grazu V., Lopez-Gallego F., Hermoso J.A., Garci{dotless}a J.L., Manso I., et al. Genetic modification of the Penicillin G Acylase surface to improve its reversible immobilization on ionic exchangers. Appl Environ Microbiol 73 (2007) 312-319
    • (2007) Appl Environ Microbiol , vol.73 , pp. 312-319
    • Montes, T.1    Grazu, V.2    Lopez-Gallego, F.3    Hermoso, J.A.4    Garcia, J.L.5    Manso, I.6
  • 83
    • 33845975312 scopus 로고    scopus 로고
    • Chemical modification of protein surfaces to improve their reversible enzyme immobilization on ionic exchangers
    • Montes T., Grazu V., Lopez-Gallego F., Hermoso J.A., Guisan J.M., and Fernandez-Lafuente R. Chemical modification of protein surfaces to improve their reversible enzyme immobilization on ionic exchangers. Biomacromolecules 7 (2006) 3052-3058
    • (2006) Biomacromolecules , vol.7 , pp. 3052-3058
    • Montes, T.1    Grazu, V.2    Lopez-Gallego, F.3    Hermoso, J.A.4    Guisan, J.M.5    Fernandez-Lafuente, R.6
  • 84
    • 0025363641 scopus 로고
    • Thermostability of (-chymotrypsin encapsulated in reversed micelle
    • Serralheiro M.L., Empis J.M., and Cabral J.M.S. Thermostability of (-chymotrypsin encapsulated in reversed micelle. Biotechnol Lett 12 (1990) 167-172
    • (1990) Biotechnol Lett , vol.12 , pp. 167-172
    • Serralheiro, M.L.1    Empis, J.M.2    Cabral, J.M.S.3
  • 85
    • 0035907129 scopus 로고    scopus 로고
    • Stability of an extreme halophilic alkaline phosphatase from Halobacterium salinarium in non-conventional medium
    • Marhuenda-Egea F.C., Piera-Velázquez S., Cadenas C., and Cadenas E. Stability of an extreme halophilic alkaline phosphatase from Halobacterium salinarium in non-conventional medium. J Biotechnol 87 (2001) 255-261
    • (2001) J Biotechnol , vol.87 , pp. 255-261
    • Marhuenda-Egea, F.C.1    Piera-Velázquez, S.2    Cadenas, C.3    Cadenas, E.4
  • 87
    • 41649097552 scopus 로고    scopus 로고
    • One-dimensional crosslinked enzyme aggregates in SBA-15: superior catalytic behavior to conventional enzyme immobilization
    • Kim M., Kim J., Lee J., Shin S., Na H.B., Hyeon T., et al. One-dimensional crosslinked enzyme aggregates in SBA-15: superior catalytic behavior to conventional enzyme immobilization. Micropor Mesopor Mater 111 (2008) 18-23
    • (2008) Micropor Mesopor Mater , vol.111 , pp. 18-23
    • Kim, M.1    Kim, J.2    Lee, J.3    Shin, S.4    Na, H.B.5    Hyeon, T.6
  • 88
    • 0035931490 scopus 로고    scopus 로고
    • Cross-linked aggregates of penicillin acylase: robust catalysts for the synthesis of β-lactam antibiotics
    • Cao L., Van Langen L.M., Van Rantwijk F., and Sheldon R.A. Cross-linked aggregates of penicillin acylase: robust catalysts for the synthesis of β-lactam antibiotics. J Mol Catal B: Enzymatic 11 (2001) 665-670
    • (2001) J Mol Catal B: Enzymatic , vol.11 , pp. 665-670
    • Cao, L.1    Van Langen, L.M.2    Van Rantwijk, F.3    Sheldon, R.A.4
  • 89
    • 0033179495 scopus 로고    scopus 로고
    • Crosslinking of enzymes for improved stability and performance
    • Govardhan C.P. Crosslinking of enzymes for improved stability and performance. Curr Opinion Biotechnol 10 (1999) 331-335
    • (1999) Curr Opinion Biotechnol , vol.10 , pp. 331-335
    • Govardhan, C.P.1
  • 90
    • 0027675591 scopus 로고
    • Borate ion-assisted stabilization of (-galactosidase from A. oryzae by polyhydroxy compounds in water miscible organic solvents
    • Shubhada S., and Sundaram P.V. Borate ion-assisted stabilization of (-galactosidase from A. oryzae by polyhydroxy compounds in water miscible organic solvents. Enzyme Microb Technol 15 (1993) 881-886
    • (1993) Enzyme Microb Technol , vol.15 , pp. 881-886
    • Shubhada, S.1    Sundaram, P.V.2
  • 91
    • 0035904878 scopus 로고    scopus 로고
    • Stabilization of various α-chymotrypsin forms in aqueous-organic media by additives
    • Laszlo K., Szava A., and Simon L.M. Stabilization of various α-chymotrypsin forms in aqueous-organic media by additives. J Mol Catal B: Enzymatic 16 (2001) 141-146
    • (2001) J Mol Catal B: Enzymatic , vol.16 , pp. 141-146
    • Laszlo, K.1    Szava, A.2    Simon, L.M.3
  • 92
    • 33644807116 scopus 로고    scopus 로고
    • A stable three-enzyme creatinine biosensor 3. Immobilization of creatinine amidohydrolase and sensor development
    • Berberich J.A., Chan A., Boden M., and Russell A.J. A stable three-enzyme creatinine biosensor 3. Immobilization of creatinine amidohydrolase and sensor development. Acta Biomater 1 (2005) 193-199
    • (2005) Acta Biomater , vol.1 , pp. 193-199
    • Berberich, J.A.1    Chan, A.2    Boden, M.3    Russell, A.J.4
  • 93
    • 27844536480 scopus 로고    scopus 로고
    • Horseradish peroxidase thermostabilization: the combinatorial effects of the surface modification and the polyols
    • Hassani L., Ranjbar B., Khajeh K., Naderi-Manesh H., Naderi-Manesh M., and Sadeghi M. Horseradish peroxidase thermostabilization: the combinatorial effects of the surface modification and the polyols. Enzyme Microb Technol 38 (2006) 118-125
    • (2006) Enzyme Microb Technol , vol.38 , pp. 118-125
    • Hassani, L.1    Ranjbar, B.2    Khajeh, K.3    Naderi-Manesh, H.4    Naderi-Manesh, M.5    Sadeghi, M.6
  • 94
    • 33644536734 scopus 로고    scopus 로고
    • Chemical modification of papain for use in alkaline medium
    • Sangeetha K., and Abraham T.E. Chemical modification of papain for use in alkaline medium. J Mol Catal B: Enzymatic 38 (2006) 171-177
    • (2006) J Mol Catal B: Enzymatic , vol.38 , pp. 171-177
    • Sangeetha, K.1    Abraham, T.E.2
  • 96
    • 0032857545 scopus 로고    scopus 로고
    • Cloning of an α-glucosidase gene from Thermococcus hydrothermalis by functional complementation of a Saccharomyces cerevisiae mal11 mutant strain
    • Galichet A., and Belarbi A. Cloning of an α-glucosidase gene from Thermococcus hydrothermalis by functional complementation of a Saccharomyces cerevisiae mal11 mutant strain. FEBS Lett 458 (1999) 188-192
    • (1999) FEBS Lett , vol.458 , pp. 188-192
    • Galichet, A.1    Belarbi, A.2
  • 97
    • 0034302593 scopus 로고    scopus 로고
    • Cloning and expression of the gene encoding thermostable poly(3-hydroxybutyrate) depolymerase
    • Takeda M., Kitashima K., Adachi K., Hanaoka Y., Suzuki I., and Koizumi J. Cloning and expression of the gene encoding thermostable poly(3-hydroxybutyrate) depolymerase. J Biosci Bioeng 90 (2000) 416-421
    • (2000) J Biosci Bioeng , vol.90 , pp. 416-421
    • Takeda, M.1    Kitashima, K.2    Adachi, K.3    Hanaoka, Y.4    Suzuki, I.5    Koizumi, J.6
  • 98
    • 0034507457 scopus 로고    scopus 로고
    • Cloning and expression of the gene encoding the thermophilic NAD(P)H-FMN oxidoreductase coupling with the desulfurization enzymes from Paenibacillus sp. Al l-2
    • Ishii Y., Konishi J., Suzuki M., and Maruhashi K. Cloning and expression of the gene encoding the thermophilic NAD(P)H-FMN oxidoreductase coupling with the desulfurization enzymes from Paenibacillus sp. Al l-2. J Biosci Bioeng 90 (2000) 591-599
    • (2000) J Biosci Bioeng , vol.90 , pp. 591-599
    • Ishii, Y.1    Konishi, J.2    Suzuki, M.3    Maruhashi, K.4
  • 99
    • 0029899822 scopus 로고    scopus 로고
    • The cloning, expression and crystallisation of a thermostable arginase
    • Bewley M.C., Lott J.S., Baker E.N., and Patchett M.L. The cloning, expression and crystallisation of a thermostable arginase. FEBS Lett 386 (1996) 215-218
    • (1996) FEBS Lett , vol.386 , pp. 215-218
    • Bewley, M.C.1    Lott, J.S.2    Baker, E.N.3    Patchett, M.L.4
  • 100
    • 33745936224 scopus 로고    scopus 로고
    • Cloning, expression, partial characterization and structural modeling of a novel esterase from Pyrococcus furiosus
    • Almeida R.V., Alqueres C.M., Larentis A.L., Rossle S.C., Cardoso A.M., Almeida W.I., et al. Cloning, expression, partial characterization and structural modeling of a novel esterase from Pyrococcus furiosus. Enzyme Microb Technol 39 (2006) 1128-1136
    • (2006) Enzyme Microb Technol , vol.39 , pp. 1128-1136
    • Almeida, R.V.1    Alqueres, C.M.2    Larentis, A.L.3    Rossle, S.C.4    Cardoso, A.M.5    Almeida, W.I.6
  • 101
    • 33746738274 scopus 로고    scopus 로고
    • Purification, characterization and gene cloning of thermophilic cytochrome cd1 nitrite reductase from Hydrogenobacter thermophilus TK-6
    • Suzuki M., Hirai T., Arai H., Ishii M., and Igarash Y. Purification, characterization and gene cloning of thermophilic cytochrome cd1 nitrite reductase from Hydrogenobacter thermophilus TK-6. J Biosci Bioeng 101 (2006) 391-397
    • (2006) J Biosci Bioeng , vol.101 , pp. 391-397
    • Suzuki, M.1    Hirai, T.2    Arai, H.3    Ishii, M.4    Igarash, Y.5
  • 102
    • 0038509175 scopus 로고    scopus 로고
    • Purification, characterization and gene cloning of thermostable O-acetyl-l-serine sulfhydrylase forming P-cyano-l-alanine
    • Omura H., Kuroda M., Kobayashi M., Shimizu S., Yoshida T., and Nagasawa T. Purification, characterization and gene cloning of thermostable O-acetyl-l-serine sulfhydrylase forming P-cyano-l-alanine. J Biosci Bioeng 95 (2003) 470-475
    • (2003) J Biosci Bioeng , vol.95 , pp. 470-475
    • Omura, H.1    Kuroda, M.2    Kobayashi, M.3    Shimizu, S.4    Yoshida, T.5    Nagasawa, T.6
  • 103
    • 0037125257 scopus 로고    scopus 로고
    • Application of a thermostable glutamate racemase from Bacillus sp. SK-1 for the production of d-phenylalanine in a multi-enzyme system
    • Bae H., Hong S., Lee S., Kwak M., Esaki N., and Sung M. Application of a thermostable glutamate racemase from Bacillus sp. SK-1 for the production of d-phenylalanine in a multi-enzyme system. J Mol Catal B: Enzymatic 17 (2002) 223-233
    • (2002) J Mol Catal B: Enzymatic , vol.17 , pp. 223-233
    • Bae, H.1    Hong, S.2    Lee, S.3    Kwak, M.4    Esaki, N.5    Sung, M.6
  • 104
    • 0034029329 scopus 로고    scopus 로고
    • Isolation, characterization, and molecular cloning of a thermostable xylitol oxidase from Streptomyces sp. IKD472
    • Yamashita M., Omura H., Okamot E., Furuya Y., Yabuuchi M., Fukahi K., et al. Isolation, characterization, and molecular cloning of a thermostable xylitol oxidase from Streptomyces sp. IKD472. J Biosci Bioeng 89 (2000) 350-360
    • (2000) J Biosci Bioeng , vol.89 , pp. 350-360
    • Yamashita, M.1    Omura, H.2    Okamot, E.3    Furuya, Y.4    Yabuuchi, M.5    Fukahi, K.6
  • 105
    • 0035840051 scopus 로고    scopus 로고
    • Cloning and overexpression of the oah1 gene encoding O-acetyl-l-homoserine sulfhydrylase of Thermus thermophilus HB8 and characterization of the gene product
    • Shimizu H., Yamagata S., Masui R., Inoue Y., Shibata T., Yokoyama S., et al. Cloning and overexpression of the oah1 gene encoding O-acetyl-l-homoserine sulfhydrylase of Thermus thermophilus HB8 and characterization of the gene product. Biochim Biophys Acta (BBA) - Protein Struct Mol Enzymol 1549 (2001) 61-72
    • (2001) Biochim Biophys Acta (BBA) - Protein Struct Mol Enzymol , vol.1549 , pp. 61-72
    • Shimizu, H.1    Yamagata, S.2    Masui, R.3    Inoue, Y.4    Shibata, T.5    Yokoyama, S.6
  • 106
    • 0037458157 scopus 로고    scopus 로고
    • Development of a genetic system for hyperthermophilic Archaea: expression of a moderate thermophilic bacterial alcohol dehydrogenase gene in Sulfolobus solfataricus
    • Contursi P., Cannio R., Prato S., Fiorentino G., Rossi M., and Bartolucci S. Development of a genetic system for hyperthermophilic Archaea: expression of a moderate thermophilic bacterial alcohol dehydrogenase gene in Sulfolobus solfataricus. FEMS Microbiol Lett 218 (2003) 115-120
    • (2003) FEMS Microbiol Lett , vol.218 , pp. 115-120
    • Contursi, P.1    Cannio, R.2    Prato, S.3    Fiorentino, G.4    Rossi, M.5    Bartolucci, S.6
  • 107
    • 8844286155 scopus 로고    scopus 로고
    • Expression in Trichoderma reesei and characterisation of a thermostable family 3 β-glucosidase from the moderately thermophilic fungus Talaromyces emersonii
    • Murray P., Aro N., Collins C., Grassick A., Penttila M., Saloheimo M., et al. Expression in Trichoderma reesei and characterisation of a thermostable family 3 β-glucosidase from the moderately thermophilic fungus Talaromyces emersonii. Prot Exp Puri 38 (2004) 248-257
    • (2004) Prot Exp Puri , vol.38 , pp. 248-257
    • Murray, P.1    Aro, N.2    Collins, C.3    Grassick, A.4    Penttila, M.5    Saloheimo, M.6
  • 108
    • 13844320315 scopus 로고    scopus 로고
    • A recombinant exonuclease III homologue of the thermophilic archaeon Methanothermobacter thermautotrophicus
    • Pfeifer S., and Greiner-Stoffele T. A recombinant exonuclease III homologue of the thermophilic archaeon Methanothermobacter thermautotrophicus. DNA Repair 4 (2005) 433-444
    • (2005) DNA Repair , vol.4 , pp. 433-444
    • Pfeifer, S.1    Greiner-Stoffele, T.2
  • 109
    • 20444408450 scopus 로고    scopus 로고
    • Characterization of thermostable lipase from thermophilic Geobacillus sp. TW1
    • Li H., and Zhang X. Characterization of thermostable lipase from thermophilic Geobacillus sp. TW1. Prot Exp Puri 42 (2005) 153-159
    • (2005) Prot Exp Puri , vol.42 , pp. 153-159
    • Li, H.1    Zhang, X.2
  • 110
    • 0035717165 scopus 로고    scopus 로고
    • Molecular cloning expression, purification, and characterization of fructose-1.6-bisphosphate aldolase from Thermus aquaticus
    • Sauve V., and Sygusch J. Molecular cloning expression, purification, and characterization of fructose-1.6-bisphosphate aldolase from Thermus aquaticus. Prot Exp Puri 21 (2001) 293-302
    • (2001) Prot Exp Puri , vol.21 , pp. 293-302
    • Sauve, V.1    Sygusch, J.2
  • 111
    • 2542510221 scopus 로고    scopus 로고
    • Cloning and expression of an α-amylase encoding gene from the hyperthermophilic archaebacterium Thermococcus hydrothermalis and biochemical characterisation of the recombinant enzyme
    • Leveque E., Haye B., and Belarbi A. Cloning and expression of an α-amylase encoding gene from the hyperthermophilic archaebacterium Thermococcus hydrothermalis and biochemical characterisation of the recombinant enzyme. FEMS Microbiol Lett 186 (2000) 67-71
    • (2000) FEMS Microbiol Lett , vol.186 , pp. 67-71
    • Leveque, E.1    Haye, B.2    Belarbi, A.3
  • 112
    • 0037469277 scopus 로고    scopus 로고
    • Cloning, expression and evolution of the gene encoding the elongation factor 1α from a low thermophilic Sulfolobus solfataricus strain
    • Masullo M., Cantiello P., Lamberti A., Longo O., Fiengo A., and Arcari P. Cloning, expression and evolution of the gene encoding the elongation factor 1α from a low thermophilic Sulfolobus solfataricus strain. FEMS Microbiol Lett 218 (2003) 285-290
    • (2003) FEMS Microbiol Lett , vol.218 , pp. 285-290
    • Masullo, M.1    Cantiello, P.2    Lamberti, A.3    Longo, O.4    Fiengo, A.5    Arcari, P.6
  • 113
    • 0038705903 scopus 로고    scopus 로고
    • Cloning, structural analysis and expression of the gene encoding aspartate aminotransferase from the thermophilic cyanobacterium Phormidium lapideum
    • Kim H., Nakaoka M., Mayumi Yagi M., Ashida H., Hamada K., Shibata H., et al. Cloning, structural analysis and expression of the gene encoding aspartate aminotransferase from the thermophilic cyanobacterium Phormidium lapideum. J Biosci Bioeng 95 (2003) 421-424
    • (2003) J Biosci Bioeng , vol.95 , pp. 421-424
    • Kim, H.1    Nakaoka, M.2    Mayumi Yagi, M.3    Ashida, H.4    Hamada, K.5    Shibata, H.6
  • 117
    • 33751164160 scopus 로고    scopus 로고
    • Selective adsorption of large proteins on highly activated IMAC supports in the presence of high imidazole concentrations: purification, reversible immobilization and stabilization of thermophilic α- and β-galactosidases
    • Pessela B.C., Mateo C., Filho M., Carrascosa A., Fernandez-Lafuente R., and Guisan J.M. Selective adsorption of large proteins on highly activated IMAC supports in the presence of high imidazole concentrations: purification, reversible immobilization and stabilization of thermophilic α- and β-galactosidases. Enzyme Microb Technol 40 (2007) 242-248
    • (2007) Enzyme Microb Technol , vol.40 , pp. 242-248
    • Pessela, B.C.1    Mateo, C.2    Filho, M.3    Carrascosa, A.4    Fernandez-Lafuente, R.5    Guisan, J.M.6
  • 120
    • 0028835759 scopus 로고
    • The use of stabilised penicillin acylase derivatives improves the design of kinetically controlled synthesis
    • Fernandez-Lafuente R., Rosell C.M., and Guisan J.M. The use of stabilised penicillin acylase derivatives improves the design of kinetically controlled synthesis. J Mol Catal A: Chem 101 (1995) 91-97
    • (1995) J Mol Catal A: Chem , vol.101 , pp. 91-97
    • Fernandez-Lafuente, R.1    Rosell, C.M.2    Guisan, J.M.3
  • 121
    • 12344312508 scopus 로고    scopus 로고
    • Improved stabilization of chemically aminated enzymes via multipoint covalent attachment on glyoxyl supports
    • Lopez-Gallego F., Montes T., Fuentes M., Alonso N., Grazu V., Betancor L., et al. Improved stabilization of chemically aminated enzymes via multipoint covalent attachment on glyoxyl supports. J Biotechnol 116 (2005) 1-10
    • (2005) J Biotechnol , vol.116 , pp. 1-10
    • Lopez-Gallego, F.1    Montes, T.2    Fuentes, M.3    Alonso, N.4    Grazu, V.5    Betancor, L.6
  • 123
    • 33847290758 scopus 로고    scopus 로고
    • Evaluation of different immobilization strategies to prepare an industrial biocatalyst of formate dehydrogenase from Candida boidinii
    • Bolivar J.M., Wilson L., Ferrarotti S.A., Fernandez-Lafuente R., Guisan J.M., and Mateo C. Evaluation of different immobilization strategies to prepare an industrial biocatalyst of formate dehydrogenase from Candida boidinii. Enzyme Microb Technol 40 (2007) 540-546
    • (2007) Enzyme Microb Technol , vol.40 , pp. 540-546
    • Bolivar, J.M.1    Wilson, L.2    Ferrarotti, S.A.3    Fernandez-Lafuente, R.4    Guisan, J.M.5    Mateo, C.6
  • 126
    • 33645222148 scopus 로고    scopus 로고
    • Improvement of the functional properties of a thermostable lipase from Alcaligenes sp. via strong adsorption on hydrophobic supports
    • Wilson L., Palomo J.M., Fernandez-Lorente G., Illanes A., Guisan J.M., and Fernandez-Lafuente R. Improvement of the functional properties of a thermostable lipase from Alcaligenes sp. via strong adsorption on hydrophobic supports. Enzyme Microb Technol 38 (2006) 975-980
    • (2006) Enzyme Microb Technol , vol.38 , pp. 975-980
    • Wilson, L.1    Palomo, J.M.2    Fernandez-Lorente, G.3    Illanes, A.4    Guisan, J.M.5    Fernandez-Lafuente, R.6
  • 127
    • 0142075810 scopus 로고    scopus 로고
    • Design of an immobilized preparation of catalase from Thermus thermophilus to be used in a wide range of conditions, structural stabilization of a multimeric enzyme
    • Hidalgo A., Betancor L., Lopez-Gallego F., Morenob R., Berenguer J., Fernandez-Lafuente R., et al. Design of an immobilized preparation of catalase from Thermus thermophilus to be used in a wide range of conditions, structural stabilization of a multimeric enzyme. Enzyme Microb Technol 33 (2003) 278-285
    • (2003) Enzyme Microb Technol , vol.33 , pp. 278-285
    • Hidalgo, A.1    Betancor, L.2    Lopez-Gallego, F.3    Morenob, R.4    Berenguer, J.5    Fernandez-Lafuente, R.6
  • 128
    • 34047274590 scopus 로고    scopus 로고
    • Hydrophilization of immobilized model enzymes suggests a widely applicable method for enhancing protein stability in polar organic co-solvents
    • Irazoqui G., Giacomini C., Batista-Viera F., and Brena B.M. Hydrophilization of immobilized model enzymes suggests a widely applicable method for enhancing protein stability in polar organic co-solvents. J Mol Catal B: Enzymatic 46 (2007) 43-51
    • (2007) J Mol Catal B: Enzymatic , vol.46 , pp. 43-51
    • Irazoqui, G.1    Giacomini, C.2    Batista-Viera, F.3    Brena, B.M.4
  • 129
    • 33746109598 scopus 로고    scopus 로고
    • Properties of catechol 1.2-dioxygenase from Pseudomonas putida immobilized in calcium alginate hydrogels
    • Kalogeris E., Sanakis Y., Mamma D., Christakopoulos P., Kekos D., and Stamatis H. Properties of catechol 1.2-dioxygenase from Pseudomonas putida immobilized in calcium alginate hydrogels. Enzyme Microb Technol 39 (2006) 1113-1121
    • (2006) Enzyme Microb Technol , vol.39 , pp. 1113-1121
    • Kalogeris, E.1    Sanakis, Y.2    Mamma, D.3    Christakopoulos, P.4    Kekos, D.5    Stamatis, H.6
  • 130
    • 34548461155 scopus 로고    scopus 로고
    • Stabilization of quaternary structure and activity of bovine liver catalase through encapsulation in liposomes
    • Yoshimoto M., Sakamoto H., Yoshimoto N., Kuboi R., and Nakao K. Stabilization of quaternary structure and activity of bovine liver catalase through encapsulation in liposomes. Enzyme Microb Technol 41 (2007) 849-858
    • (2007) Enzyme Microb Technol , vol.41 , pp. 849-858
    • Yoshimoto, M.1    Sakamoto, H.2    Yoshimoto, N.3    Kuboi, R.4    Nakao, K.5


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